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SUMMARY:Optical super-resolution microscopy for bacterial spore coat struc
 ture determination - James Manton
DTSTART:20160306T140500Z
DTEND:20160306T142500Z
UID:TALK64920@talks.cam.ac.uk
CONTACT:Andrew Carlotti
DESCRIPTION:Multi-layered protein coats are used for environmental protect
 ion\, sensing\, and interaction by many microorganisms\, including spore-f
 orming bacteria and viruses. In spores of Bacillus subtilis\, over 70 dist
 inct proteins make up a coat that is only about 100 nm thick\, which helps
  keep the spore viable and able to germinate after a time as long as sever
 al decades in a harsh environment. Distinguishing the order of protein lay
 ers can indicate the function of different proteins – for example\, whic
 h proteins form the outermost layers that protect the spore from lytic enz
 ymes\, and which hold the structure together? While fluorescent fusion pro
 teins provide the only practical and non-invasive way to identify specific
  proteins in these multi-layered specimens\, conventional optical microsco
 py lacks the resolution to resolve adjacent protein layers. Our original m
 ethods of fluorescent shell localisation make it possible to determine the
  order and geometry of concentric protein layers by fitting mathematical m
 odel structures to image data. Our method determines the radius of protein
  shells to a precision better than 10 nm\, and produces layer orders for B
 acillus subtilis and megaterium consistent with previous electron mi­cros
 copy studies. In addition\, the aspect ratio of elongated spores and the t
 endency of some pro­teins to localise near the poles can be quantified\, 
 enabling measurement of structural anisotropy. In future work\, this techn
 ique will be used to optimise the structure of bacterial strains being dev
 eloped for therapeutic drug delivery\, in a joint project with MedImmune.
LOCATION:Winstanley Lecture Theatre
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